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. Author manuscript; available in PMC: 2010 Jul 1.
Published in final edited form as: Cell Mol Bioeng. 2010 Jun 1;3(2):139–150. doi: 10.1007/s12195-010-0121-3

Figure 4.

Figure 4

Protein size measured by DLS for SLR2-7 and SLR2-7ΔAD as a function of increasing temperature. Protein size was measured at each indicated temperature, and average peak size was plotted; bars indicate standard deviation. Asterisks indicate that the plotted size is the average of two unresolved peaks, interpreted as a mixture of monomers and dimers at that temperature. With increasing temperature each construct changed from single-peak dimers, to presumed mixtures of dimers and monomers (asterisk), to single-peak monomers. SLR2-7ΔAD completely dissociates at near 42°C; SLR2-7 completely dissociates at near 58°C. Dissociated proteins then extended further, prior to denaturing above 54°C (SLR2-7ΔAD) or above 66°C (SLR2-7). (n=2 independent runs).